Amyloid beta-Protein Aggregation Produces Highly Reproducible Kinetic Data and Occurs by a Two-Phase Process
(2010) In ACS Chemical Neuroscience 1(1). p.13-18- Abstract
- Protein aggregation can lead to major disturbances of cellular processes and is associated with several diseases. We report kinetic and equilibrium data by ThT fluorescence and enzyme-linked immunosorbent assay of sufficient quality and reproducibility to form a basis for mechanistic understanding of amyloid beta-peptide (A beta) fibril formation. Starting from monomeric peptide in a pure buffer system without cosolvents, we find that the kinetics of A beta aggregation vary strongly with peptide concentration in a highly predictable manner. The free A beta concentration in equilibrium with fibrils was found to vary with total peptide concentration in a manner expected for a two-phase system. The free versus total A beta concentration was... (More)
- Protein aggregation can lead to major disturbances of cellular processes and is associated with several diseases. We report kinetic and equilibrium data by ThT fluorescence and enzyme-linked immunosorbent assay of sufficient quality and reproducibility to form a basis for mechanistic understanding of amyloid beta-peptide (A beta) fibril formation. Starting from monomeric peptide in a pure buffer system without cosolvents, we find that the kinetics of A beta aggregation vary strongly with peptide concentration in a highly predictable manner. The free A beta concentration in equilibrium with fibrils was found to vary with total peptide concentration in a manner expected for a two-phase system. The free versus total A beta concentration was linear up to ca. 0.2,mu M, after which free A beta decreased with total A beta toward an asymptotic value. Our results imply that A beta fibril formation arises from a sequence of events in a highly predictable manner. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1617649
- author
- Hellstrand, Erik LU ; Boland, Barry ; Walsh, Dominic M. and Linse, Sara LU
- organization
- publishing date
- 2010
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Alzheimer, mechanism, kinetics, Amyloid, aggregation, fibril
- in
- ACS Chemical Neuroscience
- volume
- 1
- issue
- 1
- pages
- 13 - 18
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- wos:000277743100003
- scopus:77951676986
- pmid:22778803
- ISSN
- 1948-7193
- DOI
- 10.1021/cn900015v
- language
- English
- LU publication?
- yes
- id
- 44ac5a93-b3e4-46ac-b657-1da13135d03f (old id 1617649)
- date added to LUP
- 2016-04-01 13:40:57
- date last changed
- 2022-04-06 06:16:43
@article{44ac5a93-b3e4-46ac-b657-1da13135d03f, abstract = {{Protein aggregation can lead to major disturbances of cellular processes and is associated with several diseases. We report kinetic and equilibrium data by ThT fluorescence and enzyme-linked immunosorbent assay of sufficient quality and reproducibility to form a basis for mechanistic understanding of amyloid beta-peptide (A beta) fibril formation. Starting from monomeric peptide in a pure buffer system without cosolvents, we find that the kinetics of A beta aggregation vary strongly with peptide concentration in a highly predictable manner. The free A beta concentration in equilibrium with fibrils was found to vary with total peptide concentration in a manner expected for a two-phase system. The free versus total A beta concentration was linear up to ca. 0.2,mu M, after which free A beta decreased with total A beta toward an asymptotic value. Our results imply that A beta fibril formation arises from a sequence of events in a highly predictable manner.}}, author = {{Hellstrand, Erik and Boland, Barry and Walsh, Dominic M. and Linse, Sara}}, issn = {{1948-7193}}, keywords = {{Alzheimer; mechanism; kinetics; Amyloid; aggregation; fibril}}, language = {{eng}}, number = {{1}}, pages = {{13--18}}, publisher = {{The American Chemical Society (ACS)}}, series = {{ACS Chemical Neuroscience}}, title = {{Amyloid beta-Protein Aggregation Produces Highly Reproducible Kinetic Data and Occurs by a Two-Phase Process}}, url = {{http://dx.doi.org/10.1021/cn900015v}}, doi = {{10.1021/cn900015v}}, volume = {{1}}, year = {{2010}}, }